次级代谢产物生物合成的调控。十七。金色链霉菌中苹果酸脱氢酶（脱羧）的纯化及性质
Regulation of biosynthesis of secondary metabolites. XVII. Purification and properties of malate dehydrogenase (decarboxylating) in Streptomyces aureofaciens.
作者信息
Jechová V, Hostálek Z, Vanĕk Z
出版信息
Folia Microbiol (Praha). 1975;20(2):137-41. doi: 10.1007/BF02876770.
The process of isolation and purification of malate dehydrogenase (decarboxylating) (EC 1.1.1.40) from the mycelium of the actinomycete Streptomyces aureofaciens has been worked out. The enzyme was purified 35 fold. The kinetic characters of the purified enzyme are very similar to the figures for malate dehydrogenase (decarboxylating) from other sources. Km for L-malate = 2.1 X 10(-3)M, Km for NADP = 4.6 X 10(-5)M (at pH 7.4). The reaction requires metal divalent ions, Mn2+ being more effective than Mg2+. The enzyme reaches its maximal activity at pH 8.75.
已研究出从金色链霉菌的菌丝体中分离和纯化苹果酸脱氢酶（脱羧）（EC 1.1.1.40）的方法。该酶被纯化了35倍。纯化后酶的动力学特性与其他来源的苹果酸脱氢酶（脱羧）的数据非常相似。L-苹果酸的米氏常数（Km）=2.1×10⁻³M，烟酰胺腺嘌呤二核苷酸磷酸（NADP）的米氏常数（Km）=4.6×10⁻⁵M（在pH 7.4时）。该反应需要二价金属离子，锰离子（Mn²⁺）比镁离子（Mg²⁺）更有效。该酶在pH 8.75时达到最大活性。
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